ID A0A0V0UN36_9BILA Unreviewed; 1243 AA.
AC A0A0V0UN36;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Rho guanine nucleotide exchange factor 2 {ECO:0000313|EMBL:KRX52745.1};
DE Flags: Fragment;
GN ORFNames=T09_5947 {ECO:0000313|EMBL:KRX52745.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52745.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX52745.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX52745.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX52745.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDN01000228; KRX52745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UN36; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20805; C1_DGK_rpt2; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF21; CYSTS, ISOFORM C; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 296..345
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 454..629
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 159..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 969..1029
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 889..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX52745.1"
SQ SEQUENCE 1243 AA; 138110 MW; 3D48E95DCE96FA64 CRC64;
LFKFISTAQR YHTTVLIGMK RDVSVSWPNL AEIPSRTPST SFSICCLIKS HSLTASSQSV
EACQLSFADN GVDLAATASH GVHKHFADGS RRSCSGDDGT PMKLAVDRGA PVKLSKSVEC
VVPGTVRVNL GCSKSEVDLS QLSAASRLSE KRFSLGDQSS LAQRLHDSSN EEDPAGTTAL
TANPADQQKE LLKFVDNAVH LDRSFSSTPS IDVDSSLAYF AVLPRDKPNE VSRERLRQIR
ASSMVVPAIT PRLPLMGLLP KAVGKASNDK VDLKSIEKVL KLRSSKKHAK VKEKKQHVWL
QCQEKAGLNC DICNKAEGNY SFVRCTECHA VLHSHCKAAA NKASCSRGKA ASKHSSVMFQ
TRPLSLVSRF SSFRSDSSSS VIGQIYAETS NRSGPLPQSA DCVISVLPDG AGVYTIPDEK
WAELGLWSAE ADGNWWSTGR GKVARNYMST KEVKRQDIIH ELVTTERHHC ITLVLLKHTY
FDGLLGLNIL TNDELNMLMP HLELLLEVHL HFLQLLKKKV DESFTGGVAE KMQLAYTTFC
SRKDFSVQEY HRLCQTNPNF SIFMENMNKL PYFKARSLPD CLLLVTQRLS KYHSFVESLR
KNTEDALLKD EILKAEQAVK KLVANVDQGI GDIQLQQLCK EIVAQMDTKE STTFLGKTFT
KNELLSNTRT LLHAGDVYWQ NAMRKPTEVK MLLFSDIIVF LQRVGNSYAF FSQDNKECII
SLLKLIVREK AGRSGSQGLY LISAAPSHAE MYEIICHTKK MLASWTERIQ RAVDVCPPAA
IEERPSSESV FAVEHEEQLK TLFGKVNNCN DELKKLLDCQ IEAYGEILQL VHKMNIPDEE
ERMKIMKTID ECLPAKIAAT AVARFADLMS QLVRERCKQQ LLNLACPTDT ATAQTTTSSD
GSNINRSQTF HGMRNDSKKS KLYRKRVTVS GIPQRCEENR IVETAIDNGM SGEIHADSKS
AFCAVMSRLK DAEIELDGMK HEKAMLLIEL EKEKSIRSSS AQNVYNAGLE ELRRLHSDFE
KRRSEFQQLV DEKKSDFEHR ENAIREKEER LNREDSELQS KWQCLREAWE KLQLSGVPIR
SLTSPLAPST SCAAYIATCN SSTNASNPVN HPPAGGDNSN NSGPIGKQSN STVANSTPTV
GVDDSSNITC VRSGVGISGG STSASAEKQS FRKVQVPPYL LGSFVHSGRL PDDLVRQQLP
SKLLKDDMFN SLSSRFQSSM KERRKGSPKV KDNHSINVKG KQK
//
